data_6176 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B ; _BMRB_accession_number 6176 _BMRB_flat_file_name bmr6176.str _Entry_type original _Submission_date 2004-04-13 _Accession_date 2004-04-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lytle B. L. . 2 Peterson F. C. . 3 Qui S. H. . 4 Luo M. . . 5 Volkman B. F. . 6 Markley J. L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 662 "13C chemical shifts" 502 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-07-08 update BMRB 'added time domain data' 2007-01-04 update author 'update the entry citation' 2004-06-25 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15364906 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lytle B. L. . 2 Peterson F. C. . 3 Qui S. H. . 4 Luo M. . . 5 Zhao Q. . . 6 Markley J. L. . 7 Volkman B. F. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 279 _Journal_issue 45 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 46787 _Page_last 46793 _Year 2004 _Details . loop_ _Keyword ubiquitin-like tubulin microtubule cytoskeleton chaperone 'Center for Eukaryotic Structural Genomics' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref-2 _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref-3 _Saveframe_category citation _Citation_full ; Bartels, C., Guntert, P., Billeter, M. and Wuthrich, K. (1997) J. Comp. Chem. 18, 139-149. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref-4 _Saveframe_category citation _Citation_full ; Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302. ; _Citation_title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10212987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu G . . 2 Delaglio F . . 3 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 13 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 289 _Page_last 302 _Year 1999 _Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; save_ save_ref-5 _Saveframe_category citation _Citation_full ; Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27. ; _Citation_title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12051947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Herrmann Torsten . . 2 Guntert Peter . . 3 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 319 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 209 _Page_last 227 _Year 2002 _Details ; Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination. ; save_ save_ref-6 _Saveframe_category citation _Citation_full ; Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73. ; _Citation_title 'The Xplor-NIH NMR molecular structure determination package.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12565051 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwieters 'Charles D' D. . 2 Kuszewski 'John J' J. . 3 Tjandra Nico . . 4 Clore 'G Marius' M. . stop_ _Journal_abbreviation 'J. Magn. Reson.' _Journal_name_full 'Journal of magnetic resonance (San Diego, Calif. : 1997)' _Journal_volume 160 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 65 _Page_last 73 _Year 2003 _Details ; We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis. ; save_ ################################## # Molecular system description # ################################## save_system_UBL_domain _Saveframe_category molecular_system _Mol_system_name 'Ubiquitin-like domain of tubulin-folding cofactor B' _Abbreviation_common 'UBL domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ubiquitin-like domain' $UBL_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function chaperone stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UBL_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ubiquitin-like domain of tubulin-folding cofactor B' _Abbreviation_common 'UBL domain' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; MTEVYDLEITTNATDFPMEK KYPAGMSLNDLKKKLELVVG TTVDSMRIQLFDGDDQLKGE LTDGAKSLKDLGVRDGYRIH AVDVTGGNEDFKDESMVEKY EMSDDTYGKRTDSVRAWKKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 GLU 4 VAL 5 TYR 6 ASP 7 LEU 8 GLU 9 ILE 10 THR 11 THR 12 ASN 13 ALA 14 THR 15 ASP 16 PHE 17 PRO 18 MET 19 GLU 20 LYS 21 LYS 22 TYR 23 PRO 24 ALA 25 GLY 26 MET 27 SER 28 LEU 29 ASN 30 ASP 31 LEU 32 LYS 33 LYS 34 LYS 35 LEU 36 GLU 37 LEU 38 VAL 39 VAL 40 GLY 41 THR 42 THR 43 VAL 44 ASP 45 SER 46 MET 47 ARG 48 ILE 49 GLN 50 LEU 51 PHE 52 ASP 53 GLY 54 ASP 55 ASP 56 GLN 57 LEU 58 LYS 59 GLY 60 GLU 61 LEU 62 THR 63 ASP 64 GLY 65 ALA 66 LYS 67 SER 68 LEU 69 LYS 70 ASP 71 LEU 72 GLY 73 VAL 74 ARG 75 ASP 76 GLY 77 TYR 78 ARG 79 ILE 80 HIS 81 ALA 82 VAL 83 ASP 84 VAL 85 THR 86 GLY 87 GLY 88 ASN 89 GLU 90 ASP 91 PHE 92 LYS 93 ASP 94 GLU 95 SER 96 MET 97 VAL 98 GLU 99 LYS 100 TYR 101 GLU 102 MET 103 SER 104 ASP 105 ASP 106 THR 107 TYR 108 GLY 109 LYS 110 ARG 111 THR 112 ASP 113 SER 114 VAL 115 ARG 116 ALA 117 TRP 118 LYS 119 LYS 120 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-08-17 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1T0Y "Solution Structure Of A Ubiquitin-Like Domain From Tubulin- Binding Cofactor B" 100.00 122 100.00 100.00 1.67e-79 EMBL CAB01212 "Protein TBCB-1 [Caenorhabditis elegans]" 100.00 229 100.00 100.00 3.48e-78 REF NP_506367 "Protein F53F4.3 [Caenorhabditis elegans]" 100.00 229 100.00 100.00 3.48e-78 SP Q20728 "RecName: Full=Tubulin-specific chaperone B; AltName: Full=Tubulin-folding cofactor B; Short=CoB [Caenorhabditis elegans]" 100.00 229 100.00 100.00 3.48e-78 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $UBL_domain 'C. elegans' 6239 Eukaryota Metazoa Caenorhabditis elegans '5O73 (F53F4.3)' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $UBL_domain 'recombinant technology' 'E. coli' Escherichia coli SG13009[pREP4] plasmid pQE30T 'pQE30T is pQE30 (Qiagen) modified to contain a TEV protease site.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UBL_domain 1 mM '[U-13C; U-15N]' NaCl 50 mM . 'sodium phosphate buffer' 20 mM . H20 90 % . D20 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 loop_ _Task collection stop_ _Details 'Bruker Biospin' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.1 loop_ _Task processing stop_ _Details . _Citation_label $ref-1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.1 loop_ _Task analysis stop_ _Details . _Citation_label $ref-2 save_ save_SPSCAN _Saveframe_category software _Name SPSCAN _Version 1.1.0 loop_ _Task 'peak picking' stop_ _Details 'Ralf W. Glaser' save_ save_GARANT _Saveframe_category software _Name GARANT _Version 2.1 loop_ _Task 'automated backbone assignments' stop_ _Details . _Citation_label $ref-3 save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Task 'generation of torsion angle restraints' stop_ _Details . _Citation_label $ref-4 save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0.6 loop_ _Task 'refinement (torsion angle dynamics)' stop_ _Details 'CANDID module used for automated NOE crosspeak assignment' _Citation_label $ref-5 save_ save_XPLOR-NIH _Saveframe_category software _Name XPLOR-NIH _Version 2.0.6 loop_ _Task 'refinement (cartesian MD in explicit solvent)' stop_ _Details . _Citation_label $ref-6 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_3D_15N-NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY' _Sample_label $sample_1 save_ save_3D_13C-NOESY-aliphatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aliphatic' _Sample_label $sample_1 save_ save_3D_13C-NOESY-aromatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aromatic' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aliphatic' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aromatic' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 298 . K 'ionic strength' 70 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ubiquitin-like domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET N N 122.5 0.15 1 2 . 1 MET H H 8.61 0.02 1 3 . 1 MET CA C 55.6 0.15 1 4 . 1 MET CB C 32.9 0.15 1 5 . 1 MET CG C 32.7 0.15 1 6 . 1 MET C C 176.3 0.15 1 7 . 2 THR N N 116.3 0.15 1 8 . 2 THR H H 8.11 0.02 1 9 . 2 THR CA C 62.4 0.15 1 10 . 2 THR HA H 4.20 0.02 1 11 . 2 THR CB C 69.7 0.15 1 12 . 2 THR HB H 4.21 0.02 1 13 . 2 THR HG2 H 1.13 0.02 1 14 . 2 THR CG2 C 21.8 0.15 1 15 . 2 THR C C 174.0 0.15 1 16 . 3 GLU N N 125.4 0.15 1 17 . 3 GLU H H 8.34 0.02 1 18 . 3 GLU CA C 56.8 0.15 1 19 . 3 GLU HA H 4.23 0.02 1 20 . 3 GLU CB C 30.5 0.15 1 21 . 3 GLU HB2 H 1.79 0.02 1 22 . 3 GLU HB3 H 1.79 0.02 1 23 . 3 GLU CG C 36.3 0.15 1 24 . 3 GLU HG2 H 2.19 0.02 2 25 . 3 GLU HG3 H 1.89 0.02 2 26 . 3 GLU C C 175.5 0.15 1 27 . 4 VAL N N 123.7 0.15 1 28 . 4 VAL H H 8.38 0.02 1 29 . 4 VAL CA C 60.4 0.15 1 30 . 4 VAL HA H 4.37 0.02 1 31 . 4 VAL CB C 35.7 0.15 1 32 . 4 VAL HB H 1.71 0.02 1 33 . 4 VAL HG1 H 0.63 0.02 2 34 . 4 VAL HG2 H 0.71 0.02 2 35 . 4 VAL CG1 C 21.5 0.15 1 36 . 4 VAL CG2 C 20.2 0.15 1 37 . 4 VAL C C 174.6 0.15 1 38 . 5 TYR N N 123.6 0.15 1 39 . 5 TYR H H 8.86 0.02 1 40 . 5 TYR CA C 53.7 0.15 1 41 . 5 TYR HA H 5.41 0.02 1 42 . 5 TYR CB C 40.7 0.15 1 43 . 5 TYR HB2 H 2.74 0.02 2 44 . 5 TYR HB3 H 2.59 0.02 2 45 . 5 TYR HD1 H 6.71 0.02 1 46 . 5 TYR HD2 H 6.71 0.02 1 47 . 5 TYR HE1 H 6.44 0.02 1 48 . 5 TYR HE2 H 6.44 0.02 1 49 . 5 TYR CD1 C 130.5 0.15 1 50 . 5 TYR CE1 C 118.5 0.15 1 51 . 5 TYR C C 174.9 0.15 1 52 . 6 ASP N N 123.9 0.15 1 53 . 6 ASP H H 9.24 0.02 1 54 . 6 ASP CA C 54.2 0.15 1 55 . 6 ASP HA H 4.96 0.02 1 56 . 6 ASP CB C 40.9 0.15 1 57 . 6 ASP HB2 H 2.78 0.02 2 58 . 6 ASP HB3 H 2.61 0.02 2 59 . 6 ASP C C 175.1 0.15 1 60 . 7 LEU N N 125.3 0.15 1 61 . 7 LEU H H 8.92 0.02 1 62 . 7 LEU CA C 53.5 0.15 1 63 . 7 LEU HA H 5.16 0.02 1 64 . 7 LEU CB C 46.2 0.15 1 65 . 7 LEU HB2 H 1.65 0.02 2 66 . 7 LEU HB3 H 1.36 0.02 2 67 . 7 LEU CG C 26.7 0.15 1 68 . 7 LEU HG H 1.66 0.02 1 69 . 7 LEU HD1 H 0.87 0.02 2 70 . 7 LEU HD2 H 0.79 0.02 2 71 . 7 LEU CD1 C 26.3 0.15 1 72 . 7 LEU CD2 C 25.0 0.15 1 73 . 7 LEU C C 176.2 0.15 1 74 . 8 GLU N N 120.4 0.15 1 75 . 8 GLU H H 8.12 0.02 1 76 . 8 GLU CA C 54.8 0.15 1 77 . 8 GLU HA H 5.04 0.02 1 78 . 8 GLU CB C 32.3 0.15 1 79 . 8 GLU HB2 H 1.87 0.02 2 80 . 8 GLU HB3 H 1.82 0.02 2 81 . 8 GLU CG C 36.4 0.15 1 82 . 8 GLU C C 174.9 0.15 1 83 . 9 ILE N N 124.5 0.15 1 84 . 9 ILE H H 9.13 0.02 1 85 . 9 ILE CA C 58.5 0.15 1 86 . 9 ILE HA H 5.53 0.02 1 87 . 9 ILE CB C 39.2 0.15 1 88 . 9 ILE HB H 2.00 0.02 1 89 . 9 ILE HG2 H 0.84 0.02 1 90 . 9 ILE CG2 C 17.9 0.15 1 91 . 9 ILE CG1 C 28.1 0.15 1 92 . 9 ILE HG12 H 1.50 0.02 2 93 . 9 ILE HG13 H 1.44 0.02 2 94 . 9 ILE HD1 H 0.85 0.02 1 95 . 9 ILE CD1 C 12.4 0.15 1 96 . 9 ILE C C 176.6 0.15 1 97 . 10 THR N N 119.4 0.15 1 98 . 10 THR H H 9.47 0.02 1 99 . 10 THR CA C 60.1 0.15 1 100 . 10 THR HA H 4.84 0.02 1 101 . 10 THR CB C 71.3 0.15 1 102 . 10 THR HB H 4.55 0.02 1 103 . 10 THR HG2 H 1.02 0.02 1 104 . 10 THR CG2 C 22.4 0.15 1 105 . 10 THR C C 173.4 0.15 1 106 . 11 THR N N 109.4 0.15 1 107 . 11 THR H H 8.35 0.02 1 108 . 11 THR CA C 59.6 0.15 1 109 . 11 THR HA H 5.12 0.02 1 110 . 11 THR CB C 72.3 0.15 1 111 . 11 THR HB H 4.51 0.02 1 112 . 11 THR HG2 H 1.10 0.02 1 113 . 11 THR CG2 C 21.2 0.15 1 114 . 11 THR C C 174.5 0.15 1 115 . 12 ASN N N 116.7 0.15 1 116 . 12 ASN H H 8.50 0.02 1 117 . 12 ASN CA C 54.5 0.15 1 118 . 12 ASN HA H 4.83 0.02 1 119 . 12 ASN CB C 38.4 0.15 1 120 . 12 ASN HB2 H 3.08 0.02 2 121 . 12 ASN HB3 H 2.82 0.02 2 122 . 12 ASN ND2 N 114.6 0.15 1 123 . 12 ASN HD21 H 7.97 0.02 2 124 . 12 ASN HD22 H 7.35 0.02 2 125 . 12 ASN C C 175.2 0.15 1 126 . 13 ALA N N 122.0 0.15 1 127 . 13 ALA H H 8.42 0.02 1 128 . 13 ALA CA C 52.7 0.15 1 129 . 13 ALA HA H 4.48 0.02 1 130 . 13 ALA HB H 1.43 0.02 1 131 . 13 ALA CB C 20.8 0.15 1 132 . 13 ALA C C 177.1 0.15 1 133 . 14 THR N N 110.1 0.15 1 134 . 14 THR H H 7.32 0.02 1 135 . 14 THR CA C 60.2 0.15 1 136 . 14 THR HA H 4.50 0.02 1 137 . 14 THR CB C 71.0 0.15 1 138 . 14 THR HB H 4.17 0.02 1 139 . 14 THR HG2 H 1.13 0.02 1 140 . 14 THR CG2 C 21.8 0.15 1 141 . 14 THR C C 174.1 0.15 1 142 . 15 ASP N N 121.4 0.15 1 143 . 15 ASP H H 8.45 0.02 1 144 . 15 ASP CA C 54.6 0.15 1 145 . 15 ASP HA H 4.64 0.02 1 146 . 15 ASP CB C 41.2 0.15 1 147 . 15 ASP HB2 H 2.48 0.02 1 148 . 15 ASP HB3 H 2.48 0.02 1 149 . 15 ASP C C 175.5 0.15 1 150 . 16 PHE N N 118.6 0.15 1 151 . 16 PHE H H 7.63 0.02 1 152 . 16 PHE CA C 55.0 0.15 1 153 . 16 PHE HA H 5.01 0.02 1 154 . 16 PHE CB C 39.9 0.15 1 155 . 16 PHE HB2 H 3.14 0.02 2 156 . 16 PHE HB3 H 2.92 0.02 2 157 . 16 PHE HD1 H 7.27 0.02 1 158 . 16 PHE HD2 H 7.27 0.02 1 159 . 16 PHE HE1 H 7.35 0.02 1 160 . 16 PHE HE2 H 7.35 0.02 1 161 . 16 PHE CD1 C 132.6 0.15 1 162 . 16 PHE CE1 C 131.4 0.15 1 163 . 16 PHE C C 173.5 0.15 1 164 . 17 PRO CD C 50.9 0.15 1 165 . 17 PRO CA C 62.6 0.15 1 166 . 17 PRO HA H 4.64 0.02 1 167 . 17 PRO CB C 32.8 0.15 1 168 . 17 PRO HB2 H 2.01 0.02 2 169 . 17 PRO HB3 H 1.81 0.02 2 170 . 17 PRO CG C 27.3 0.15 1 171 . 17 PRO HG2 H 1.98 0.02 2 172 . 17 PRO HG3 H 1.85 0.02 2 173 . 17 PRO HD2 H 3.85 0.02 2 174 . 17 PRO HD3 H 3.60 0.02 2 175 . 17 PRO C C 176.4 0.15 1 176 . 18 MET N N 120.9 0.15 1 177 . 18 MET H H 8.86 0.02 1 178 . 18 MET CA C 54.7 0.15 1 179 . 18 MET HA H 4.68 0.02 1 180 . 18 MET CB C 36.1 0.15 1 181 . 18 MET HB2 H 2.03 0.02 1 182 . 18 MET HB3 H 2.03 0.02 1 183 . 18 MET CG C 32.2 0.15 1 184 . 18 MET HG2 H 2.58 0.02 1 185 . 18 MET HG3 H 2.58 0.02 1 186 . 18 MET C C 175.0 0.15 1 187 . 19 GLU N N 124.2 0.15 1 188 . 19 GLU H H 8.59 0.02 1 189 . 19 GLU CA C 56.0 0.15 1 190 . 19 GLU HA H 4.95 0.02 1 191 . 19 GLU CB C 30.6 0.15 1 192 . 19 GLU HB2 H 2.00 0.02 2 193 . 19 GLU HB3 H 1.93 0.02 2 194 . 19 GLU CG C 36.0 0.15 1 195 . 19 GLU HG2 H 2.27 0.02 2 196 . 19 GLU HG3 H 2.19 0.02 2 197 . 19 GLU C C 176.3 0.15 1 198 . 20 LYS N N 125.0 0.15 1 199 . 20 LYS H H 8.73 0.02 1 200 . 20 LYS CA C 54.0 0.15 1 201 . 20 LYS HA H 4.53 0.02 1 202 . 20 LYS CB C 38.2 0.15 1 203 . 20 LYS HB2 H 1.34 0.02 2 204 . 20 LYS HB3 H 1.12 0.02 2 205 . 20 LYS CG C 24.9 0.15 1 206 . 20 LYS HG2 H 1.32 0.02 2 207 . 20 LYS HG3 H 1.11 0.02 2 208 . 20 LYS CD C 28.9 0.15 1 209 . 20 LYS HD2 H 1.78 0.02 2 210 . 20 LYS HD3 H 1.54 0.02 2 211 . 20 LYS CE C 42.7 0.15 1 212 . 20 LYS C C 174.0 0.15 1 213 . 21 LYS N N 119.9 0.15 1 214 . 21 LYS H H 7.56 0.02 1 215 . 21 LYS CA C 54.8 0.15 1 216 . 21 LYS HA H 5.39 0.02 1 217 . 21 LYS CB C 34.6 0.15 1 218 . 21 LYS HB2 H 1.48 0.02 2 219 . 21 LYS HB3 H 1.31 0.02 2 220 . 21 LYS CG C 25.2 0.15 1 221 . 21 LYS HG2 H 1.29 0.02 1 222 . 21 LYS HG3 H 1.29 0.02 1 223 . 21 LYS CD C 29.7 0.15 1 224 . 21 LYS HD2 H 1.52 0.02 1 225 . 21 LYS HD3 H 1.52 0.02 1 226 . 21 LYS CE C 42.4 0.15 1 227 . 21 LYS C C 176.5 0.15 1 228 . 22 TYR N N 121.4 0.15 1 229 . 22 TYR H H 8.53 0.02 1 230 . 22 TYR CA C 54.5 0.15 1 231 . 22 TYR HA H 5.25 0.02 1 232 . 22 TYR CB C 41.7 0.15 1 233 . 22 TYR HB2 H 3.18 0.02 2 234 . 22 TYR HB3 H 2.27 0.02 2 235 . 22 TYR HD1 H 6.93 0.02 1 236 . 22 TYR HD2 H 6.93 0.02 1 237 . 22 TYR HE1 H 6.50 0.02 1 238 . 22 TYR HE2 H 6.50 0.02 1 239 . 22 TYR CD1 C 132.6 0.15 1 240 . 22 TYR CE1 C 117.7 0.15 1 241 . 22 TYR C C 172.7 0.15 1 242 . 23 PRO CD C 51.5 0.15 1 243 . 23 PRO CA C 62.7 0.15 1 244 . 23 PRO HA H 4.53 0.02 1 245 . 23 PRO CB C 32.5 0.15 1 246 . 23 PRO HB2 H 2.34 0.02 2 247 . 23 PRO HB3 H 1.94 0.02 2 248 . 23 PRO CG C 28.0 0.15 1 249 . 23 PRO HG2 H 2.21 0.02 2 250 . 23 PRO HG3 H 1.97 0.02 2 251 . 23 PRO HD2 H 4.04 0.02 2 252 . 23 PRO HD3 H 3.92 0.02 2 253 . 23 PRO C C 176.2 0.15 1 254 . 24 ALA N N 125.8 0.15 1 255 . 24 ALA H H 8.00 0.02 1 256 . 24 ALA CA C 54.6 0.15 1 257 . 24 ALA HA H 3.59 0.02 1 258 . 24 ALA HB H 0.62 0.02 1 259 . 24 ALA CB C 18.9 0.15 1 260 . 24 ALA C C 177.7 0.15 1 261 . 25 GLY N N 99.1 0.15 1 262 . 25 GLY H H 8.13 0.02 1 263 . 25 GLY CA C 44.9 0.15 1 264 . 25 GLY HA2 H 4.08 0.02 2 265 . 25 GLY HA3 H 3.57 0.02 2 266 . 25 GLY C C 174.6 0.15 1 267 . 26 MET N N 122.7 0.15 1 268 . 26 MET H H 7.42 0.02 1 269 . 26 MET CA C 56.1 0.15 1 270 . 26 MET HA H 4.25 0.02 1 271 . 26 MET CB C 34.9 0.15 1 272 . 26 MET HB2 H 2.19 0.02 2 273 . 26 MET HB3 H 2.00 0.02 2 274 . 26 MET CG C 31.8 0.15 1 275 . 26 MET HG2 H 2.95 0.02 2 276 . 26 MET HG3 H 2.42 0.02 2 277 . 26 MET C C 174.7 0.15 1 278 . 27 SER N N 121.0 0.15 1 279 . 27 SER H H 8.96 0.02 1 280 . 27 SER CA C 57.4 0.15 1 281 . 27 SER HA H 4.68 0.02 1 282 . 27 SER CB C 65.2 0.15 1 283 . 27 SER HB2 H 4.29 0.02 2 284 . 27 SER HB3 H 3.91 0.02 2 285 . 27 SER HG H 5.20 0.02 1 286 . 27 SER C C 175.8 0.15 1 287 . 28 LEU N N 122.5 0.15 1 288 . 28 LEU H H 8.32 0.02 1 289 . 28 LEU CA C 57.9 0.15 1 290 . 28 LEU HA H 3.96 0.02 1 291 . 28 LEU CB C 40.7 0.15 1 292 . 28 LEU HB2 H 2.09 0.02 2 293 . 28 LEU HB3 H 1.34 0.02 2 294 . 28 LEU CG C 27.3 0.15 1 295 . 28 LEU HG H 1.37 0.02 1 296 . 28 LEU HD1 H 0.51 0.02 2 297 . 28 LEU HD2 H 0.80 0.02 2 298 . 28 LEU CD1 C 25.4 0.15 1 299 . 28 LEU CD2 C 24.1 0.15 1 300 . 28 LEU C C 178.7 0.15 1 301 . 29 ASN N N 118.9 0.15 1 302 . 29 ASN H H 9.35 0.02 1 303 . 29 ASN CA C 56.3 0.15 1 304 . 29 ASN HA H 4.34 0.02 1 305 . 29 ASN CB C 38.0 0.15 1 306 . 29 ASN HB2 H 2.61 0.02 1 307 . 29 ASN HB3 H 2.61 0.02 1 308 . 29 ASN ND2 N 111.2 0.15 1 309 . 29 ASN HD21 H 7.51 0.02 2 310 . 29 ASN HD22 H 7.07 0.02 2 311 . 29 ASN C C 178.1 0.15 1 312 . 30 ASP N N 122.2 0.15 1 313 . 30 ASP H H 8.07 0.02 1 314 . 30 ASP CA C 57.5 0.15 1 315 . 30 ASP HA H 4.39 0.02 1 316 . 30 ASP CB C 40.4 0.15 1 317 . 30 ASP HB2 H 2.92 0.02 2 318 . 30 ASP HB3 H 2.51 0.02 2 319 . 30 ASP C C 178.9 0.15 1 320 . 31 LEU N N 123.8 0.15 1 321 . 31 LEU H H 8.19 0.02 1 322 . 31 LEU CA C 58.7 0.15 1 323 . 31 LEU HA H 3.82 0.02 1 324 . 31 LEU CB C 41.2 0.15 1 325 . 31 LEU HB2 H 2.06 0.02 2 326 . 31 LEU HB3 H 1.29 0.02 2 327 . 31 LEU CG C 27.3 0.15 1 328 . 31 LEU HG H 1.26 0.02 1 329 . 31 LEU HD1 H 0.66 0.02 2 330 . 31 LEU HD2 H 0.33 0.02 2 331 . 31 LEU CD1 C 26.3 0.15 1 332 . 31 LEU CD2 C 23.4 0.15 1 333 . 31 LEU C C 178.2 0.15 1 334 . 32 LYS N N 117.3 0.15 1 335 . 32 LYS H H 8.74 0.02 1 336 . 32 LYS CA C 61.3 0.15 1 337 . 32 LYS HA H 3.61 0.02 1 338 . 32 LYS CB C 32.5 0.15 1 339 . 32 LYS HB2 H 1.85 0.02 1 340 . 32 LYS HB3 H 1.85 0.02 1 341 . 32 LYS CG C 26.7 0.15 1 342 . 32 LYS HG2 H 1.83 0.02 2 343 . 32 LYS HG3 H 1.10 0.02 2 344 . 32 LYS CD C 29.9 0.15 1 345 . 32 LYS HD2 H 1.68 0.02 1 346 . 32 LYS HD3 H 1.68 0.02 1 347 . 32 LYS CE C 42.4 0.15 1 348 . 32 LYS HE2 H 2.98 0.02 2 349 . 32 LYS HE3 H 2.63 0.02 2 350 . 32 LYS C C 178.5 0.15 1 351 . 33 LYS N N 117.2 0.15 1 352 . 33 LYS H H 7.67 0.02 1 353 . 33 LYS CA C 58.8 0.15 1 354 . 33 LYS HA H 3.89 0.02 1 355 . 33 LYS CB C 31.9 0.15 1 356 . 33 LYS HB2 H 1.97 0.02 2 357 . 33 LYS HB3 H 1.90 0.02 2 358 . 33 LYS CG C 24.9 0.15 1 359 . 33 LYS HG2 H 1.49 0.02 1 360 . 33 LYS HG3 H 1.49 0.02 1 361 . 33 LYS CD C 29.0 0.15 1 362 . 33 LYS HD2 H 1.72 0.02 2 363 . 33 LYS HD3 H 1.62 0.02 2 364 . 33 LYS CE C 42.4 0.15 1 365 . 33 LYS HE2 H 2.94 0.02 2 366 . 33 LYS HE3 H 2.90 0.02 2 367 . 33 LYS C C 180.0 0.15 1 368 . 34 LYS N N 118.8 0.15 1 369 . 34 LYS H H 7.73 0.02 1 370 . 34 LYS CA C 58.6 0.15 1 371 . 34 LYS HA H 4.12 0.02 1 372 . 34 LYS CB C 32.1 0.15 1 373 . 34 LYS HB2 H 2.12 0.02 2 374 . 34 LYS HB3 H 2.01 0.02 2 375 . 34 LYS CG C 25.9 0.15 1 376 . 34 LYS HG2 H 1.63 0.02 2 377 . 34 LYS HG3 H 1.57 0.02 2 378 . 34 LYS CD C 29.0 0.15 1 379 . 34 LYS HD2 H 1.75 0.02 2 380 . 34 LYS HD3 H 1.63 0.02 2 381 . 34 LYS CE C 42.6 0.15 1 382 . 34 LYS HE2 H 3.06 0.02 1 383 . 34 LYS HE3 H 3.06 0.02 1 384 . 34 LYS C C 179.3 0.15 1 385 . 35 LEU N N 118.1 0.15 1 386 . 35 LEU H H 8.06 0.02 1 387 . 35 LEU CA C 55.6 0.15 1 388 . 35 LEU HA H 4.27 0.02 1 389 . 35 LEU CB C 42.5 0.15 1 390 . 35 LEU HB2 H 1.82 0.02 2 391 . 35 LEU HB3 H 1.33 0.02 2 392 . 35 LEU CG C 26.2 0.15 1 393 . 35 LEU HG H 1.82 0.02 1 394 . 35 LEU HD1 H 0.60 0.02 2 395 . 35 LEU HD2 H 0.74 0.02 2 396 . 35 LEU CD1 C 26.0 0.15 1 397 . 35 LEU CD2 C 22.8 0.15 1 398 . 35 LEU C C 178.2 0.15 1 399 . 36 GLU N N 122.7 0.15 1 400 . 36 GLU H H 7.78 0.02 1 401 . 36 GLU CA C 61.1 0.15 1 402 . 36 GLU HA H 3.94 0.02 1 403 . 36 GLU CB C 30.3 0.15 1 404 . 36 GLU HB2 H 2.17 0.02 2 405 . 36 GLU HB3 H 1.97 0.02 2 406 . 36 GLU CG C 37.7 0.15 1 407 . 36 GLU HG2 H 2.76 0.02 2 408 . 36 GLU HG3 H 2.20 0.02 2 409 . 36 GLU C C 179.3 0.15 1 410 . 37 LEU N N 116.3 0.15 1 411 . 37 LEU H H 7.79 0.02 1 412 . 37 LEU CA C 57.0 0.15 1 413 . 37 LEU HA H 4.17 0.02 1 414 . 37 LEU CB C 42.0 0.15 1 415 . 37 LEU HB2 H 1.74 0.02 2 416 . 37 LEU HB3 H 1.60 0.02 2 417 . 37 LEU CG C 27.6 0.15 1 418 . 37 LEU HG H 1.72 0.02 1 419 . 37 LEU HD1 H 0.93 0.02 2 420 . 37 LEU HD2 H 0.86 0.02 2 421 . 37 LEU CD1 C 24.9 0.15 1 422 . 37 LEU CD2 C 23.8 0.15 1 423 . 37 LEU C C 178.4 0.15 1 424 . 38 VAL N N 117.8 0.15 1 425 . 38 VAL H H 7.34 0.02 1 426 . 38 VAL CA C 64.2 0.15 1 427 . 38 VAL HA H 3.89 0.02 1 428 . 38 VAL CB C 33.0 0.15 1 429 . 38 VAL HB H 2.06 0.02 1 430 . 38 VAL HG1 H 1.00 0.02 2 431 . 38 VAL HG2 H 0.89 0.02 2 432 . 38 VAL CG1 C 21.8 0.15 1 433 . 38 VAL CG2 C 21.5 0.15 1 434 . 38 VAL C C 176.9 0.15 1 435 . 39 VAL N N 116.6 0.15 1 436 . 39 VAL H H 8.32 0.02 1 437 . 39 VAL CA C 63.3 0.15 1 438 . 39 VAL HA H 3.87 0.02 1 439 . 39 VAL CB C 33.3 0.15 1 440 . 39 VAL HB H 1.88 0.02 1 441 . 39 VAL HG1 H 0.91 0.02 2 442 . 39 VAL HG2 H 0.84 0.02 2 443 . 39 VAL CG1 C 23.1 0.15 1 444 . 39 VAL CG2 C 22.8 0.15 1 445 . 39 VAL C C 176.2 0.15 1 446 . 40 GLY N N 107.5 0.15 1 447 . 40 GLY H H 7.88 0.02 1 448 . 40 GLY CA C 46.1 0.15 1 449 . 40 GLY HA2 H 4.05 0.02 2 450 . 40 GLY HA3 H 3.75 0.02 2 451 . 40 GLY C C 174.4 0.15 1 452 . 41 THR N N 113.1 0.15 1 453 . 41 THR H H 7.33 0.02 1 454 . 41 THR CA C 60.0 0.15 1 455 . 41 THR HA H 4.52 0.02 1 456 . 41 THR CB C 70.0 0.15 1 457 . 41 THR HB H 3.87 0.02 1 458 . 41 THR HG2 H 0.98 0.02 1 459 . 41 THR CG2 C 19.2 0.15 1 460 . 41 THR C C 172.5 0.15 1 461 . 42 THR N N 110.0 0.15 1 462 . 42 THR H H 7.71 0.02 1 463 . 42 THR CA C 60.5 0.15 1 464 . 42 THR HA H 4.62 0.02 1 465 . 42 THR CB C 71.0 0.15 1 466 . 42 THR HB H 4.41 0.02 1 467 . 42 THR HG2 H 1.18 0.02 1 468 . 42 THR CG2 C 22.1 0.15 1 469 . 42 THR C C 177.7 0.15 1 470 . 43 VAL N N 116.8 0.15 1 471 . 43 VAL H H 8.90 0.02 1 472 . 43 VAL CA C 66.5 0.15 1 473 . 43 VAL HA H 3.69 0.02 1 474 . 43 VAL CB C 32.4 0.15 1 475 . 43 VAL HB H 2.08 0.02 1 476 . 43 VAL HG1 H 1.00 0.02 2 477 . 43 VAL HG2 H 0.97 0.02 2 478 . 43 VAL CG1 C 22.5 0.15 1 479 . 43 VAL CG2 C 19.9 0.15 1 480 . 43 VAL C C 177.4 0.15 1 481 . 44 ASP N N 116.8 0.15 1 482 . 44 ASP H H 8.03 0.02 1 483 . 44 ASP CA C 56.2 0.15 1 484 . 44 ASP HA H 4.47 0.02 1 485 . 44 ASP CB C 40.8 0.15 1 486 . 44 ASP HB2 H 2.69 0.02 2 487 . 44 ASP HB3 H 2.56 0.02 2 488 . 44 ASP C C 177.1 0.15 1 489 . 45 SER N N 115.5 0.15 1 490 . 45 SER H H 7.78 0.02 1 491 . 45 SER CA C 57.4 0.15 1 492 . 45 SER HA H 4.53 0.02 1 493 . 45 SER CB C 64.5 0.15 1 494 . 45 SER HB2 H 4.07 0.02 2 495 . 45 SER HB3 H 3.88 0.02 2 496 . 45 SER C C 171.6 0.15 1 497 . 46 MET N N 120.3 0.15 1 498 . 46 MET H H 7.25 0.02 1 499 . 46 MET CA C 54.6 0.15 1 500 . 46 MET HA H 5.11 0.02 1 501 . 46 MET CB C 37.2 0.15 1 502 . 46 MET HB2 H 1.96 0.02 2 503 . 46 MET HB3 H 1.82 0.02 2 504 . 46 MET CG C 30.7 0.15 1 505 . 46 MET HG2 H 2.24 0.02 2 506 . 46 MET HG3 H 2.01 0.02 2 507 . 46 MET C C 175.6 0.15 1 508 . 47 ARG N N 126.8 0.15 1 509 . 47 ARG H H 9.06 0.02 1 510 . 47 ARG CA C 54.7 0.15 1 511 . 47 ARG HA H 4.65 0.02 1 512 . 47 ARG CB C 33.2 0.15 1 513 . 47 ARG HB2 H 1.64 0.02 2 514 . 47 ARG HB3 H 1.50 0.02 2 515 . 47 ARG CG C 27.5 0.15 1 516 . 47 ARG HG2 H 1.58 0.02 2 517 . 47 ARG HG3 H 1.35 0.02 2 518 . 47 ARG CD C 43.7 0.15 1 519 . 47 ARG HD2 H 3.07 0.02 2 520 . 47 ARG HD3 H 3.00 0.02 2 521 . 47 ARG C C 174.9 0.15 1 522 . 48 ILE N N 124.8 0.15 1 523 . 48 ILE H H 9.11 0.02 1 524 . 48 ILE CA C 58.0 0.15 1 525 . 48 ILE HA H 4.95 0.02 1 526 . 48 ILE CB C 38.5 0.15 1 527 . 48 ILE HB H 2.16 0.02 1 528 . 48 ILE HG2 H 0.74 0.02 1 529 . 48 ILE CG2 C 18.6 0.15 1 530 . 48 ILE CG1 C 26.8 0.15 1 531 . 48 ILE HG12 H 1.30 0.02 2 532 . 48 ILE HG13 H 1.19 0.02 2 533 . 48 ILE HD1 H 0.65 0.02 1 534 . 48 ILE CD1 C 10.8 0.15 1 535 . 48 ILE C C 175.1 0.15 1 536 . 49 GLN N N 126.1 0.15 1 537 . 49 GLN H H 9.39 0.02 1 538 . 49 GLN CA C 54.5 0.15 1 539 . 49 GLN HA H 4.80 0.02 1 540 . 49 GLN CB C 33.7 0.15 1 541 . 49 GLN HB2 H 2.26 0.02 2 542 . 49 GLN HB3 H 1.61 0.02 2 543 . 49 GLN CG C 34.7 0.15 1 544 . 49 GLN HG2 H 2.22 0.02 2 545 . 49 GLN HG3 H 2.04 0.02 2 546 . 49 GLN NE2 N 110.4 0.15 1 547 . 49 GLN HE21 H 7.43 0.02 2 548 . 49 GLN HE22 H 6.64 0.02 2 549 . 49 GLN C C 173.4 0.15 1 550 . 50 LEU N N 122.7 0.15 1 551 . 50 LEU H H 8.35 0.02 1 552 . 50 LEU CA C 53.2 0.15 1 553 . 50 LEU HA H 5.22 0.02 1 554 . 50 LEU CB C 46.3 0.15 1 555 . 50 LEU HB2 H 1.84 0.02 2 556 . 50 LEU HB3 H 1.06 0.02 2 557 . 50 LEU CG C 26.3 0.15 1 558 . 50 LEU HG H 1.26 0.02 1 559 . 50 LEU HD1 H 0.86 0.02 2 560 . 50 LEU CD1 C 25.7 0.15 1 561 . 50 LEU C C 173.6 0.15 1 562 . 51 PHE N N 127.1 0.15 1 563 . 51 PHE H H 9.78 0.02 1 564 . 51 PHE CA C 56.0 0.15 1 565 . 51 PHE HA H 5.14 0.02 1 566 . 51 PHE CB C 43.2 0.15 1 567 . 51 PHE HB2 H 2.95 0.02 2 568 . 51 PHE HB3 H 2.71 0.02 2 569 . 51 PHE HD1 H 6.72 0.02 1 570 . 51 PHE HD2 H 6.72 0.02 1 571 . 51 PHE HE1 H 7.01 0.02 1 572 . 51 PHE HE2 H 7.01 0.02 1 573 . 51 PHE CD1 C 131.5 0.15 1 574 . 51 PHE CE1 C 131.3 0.15 1 575 . 51 PHE C C 175.1 0.15 1 576 . 52 ASP N N 118.8 0.15 1 577 . 52 ASP H H 8.24 0.02 1 578 . 52 ASP CA C 51.7 0.15 1 579 . 52 ASP HA H 2.99 0.02 1 580 . 52 ASP CB C 41.2 0.15 1 581 . 52 ASP HB2 H 2.69 0.02 2 582 . 52 ASP HB3 H 1.93 0.02 2 583 . 52 ASP C C 177.5 0.15 1 584 . 53 GLY N N 105.6 0.15 1 585 . 53 GLY H H 7.83 0.02 1 586 . 53 GLY CA C 46.5 0.15 1 587 . 53 GLY HA2 H 4.00 0.02 2 588 . 53 GLY HA3 H 3.76 0.02 2 589 . 53 GLY C C 174.8 0.15 1 590 . 54 ASP N N 120.4 0.15 1 591 . 54 ASP H H 8.08 0.02 1 592 . 54 ASP CA C 53.9 0.15 1 593 . 54 ASP HA H 4.86 0.02 1 594 . 54 ASP CB C 41.7 0.15 1 595 . 54 ASP HB2 H 2.90 0.02 2 596 . 54 ASP HB3 H 2.47 0.02 2 597 . 54 ASP C C 175.5 0.15 1 598 . 55 ASP N N 118.6 0.15 1 599 . 55 ASP H H 8.28 0.02 1 600 . 55 ASP CA C 56.1 0.15 1 601 . 55 ASP HA H 4.32 0.02 1 602 . 55 ASP CB C 40.5 0.15 1 603 . 55 ASP HB2 H 2.96 0.02 2 604 . 55 ASP HB3 H 2.40 0.02 2 605 . 55 ASP C C 174.8 0.15 1 606 . 56 GLN N N 117.3 0.15 1 607 . 56 GLN H H 8.32 0.02 1 608 . 56 GLN CA C 54.6 0.15 1 609 . 56 GLN HA H 4.40 0.02 1 610 . 56 GLN CB C 29.0 0.15 1 611 . 56 GLN HB2 H 2.06 0.02 2 612 . 56 GLN HB3 H 1.92 0.02 2 613 . 56 GLN CG C 34.5 0.15 1 614 . 56 GLN HG2 H 2.31 0.02 2 615 . 56 GLN HG3 H 2.09 0.02 2 616 . 56 GLN NE2 N 114.0 0.15 1 617 . 56 GLN HE21 H 7.59 0.02 2 618 . 56 GLN HE22 H 6.87 0.02 2 619 . 56 GLN C C 176.5 0.15 1 620 . 57 LEU N N 126.5 0.15 1 621 . 57 LEU H H 8.60 0.02 1 622 . 57 LEU CA C 56.1 0.15 1 623 . 57 LEU HA H 3.43 0.02 1 624 . 57 LEU CB C 41.6 0.15 1 625 . 57 LEU HB2 H 1.58 0.02 2 626 . 57 LEU HB3 H 1.17 0.02 2 627 . 57 LEU CG C 26.6 0.15 1 628 . 57 LEU HG H 0.95 0.02 1 629 . 57 LEU HD1 H 0.71 0.02 2 630 . 57 LEU HD2 H 0.13 0.02 2 631 . 57 LEU CD1 C 26.3 0.15 1 632 . 57 LEU CD2 C 21.8 0.15 1 633 . 57 LEU C C 177.3 0.15 1 634 . 58 LYS N N 128.4 0.15 1 635 . 58 LYS H H 9.49 0.02 1 636 . 58 LYS CA C 55.0 0.15 1 637 . 58 LYS HA H 4.38 0.02 1 638 . 58 LYS CB C 31.7 0.15 1 639 . 58 LYS HB2 H 1.86 0.02 2 640 . 58 LYS HB3 H 1.45 0.02 2 641 . 58 LYS CG C 23.8 0.15 1 642 . 58 LYS HG2 H 1.42 0.02 2 643 . 58 LYS HG3 H 1.33 0.02 2 644 . 58 LYS CD C 27.7 0.15 1 645 . 58 LYS HD2 H 1.58 0.02 1 646 . 58 LYS HD3 H 1.58 0.02 1 647 . 58 LYS CE C 41.8 0.15 1 648 . 58 LYS HE2 H 3.02 0.02 2 649 . 58 LYS HE3 H 2.94 0.02 2 650 . 58 LYS C C 177.0 0.15 1 651 . 59 GLY N N 104.5 0.15 1 652 . 59 GLY H H 6.90 0.02 1 653 . 59 GLY CA C 44.2 0.15 1 654 . 59 GLY HA2 H 4.41 0.02 2 655 . 59 GLY HA3 H 3.69 0.02 2 656 . 59 GLY C C 171.0 0.15 1 657 . 60 GLU N N 119.9 0.15 1 658 . 60 GLU H H 8.49 0.02 1 659 . 60 GLU CA C 55.1 0.15 1 660 . 60 GLU HA H 4.89 0.02 1 661 . 60 GLU CB C 30.9 0.15 1 662 . 60 GLU HB2 H 1.87 0.02 1 663 . 60 GLU HB3 H 1.87 0.02 1 664 . 60 GLU CG C 36.8 0.15 1 665 . 60 GLU HG2 H 2.35 0.02 2 666 . 60 GLU HG3 H 2.02 0.02 2 667 . 60 GLU C C 176.8 0.15 1 668 . 61 LEU N N 125.3 0.15 1 669 . 61 LEU H H 8.61 0.02 1 670 . 61 LEU CA C 53.7 0.15 1 671 . 61 LEU HA H 4.66 0.02 1 672 . 61 LEU CB C 42.1 0.15 1 673 . 61 LEU HB2 H 1.77 0.02 2 674 . 61 LEU HB3 H 1.25 0.02 2 675 . 61 LEU CG C 27.0 0.15 1 676 . 61 LEU HG H 1.54 0.02 1 677 . 61 LEU HD1 H 0.75 0.02 2 678 . 61 LEU HD2 H 0.81 0.02 2 679 . 61 LEU CD1 C 25.1 0.15 1 680 . 61 LEU CD2 C 22.5 0.15 1 681 . 61 LEU C C 176.2 0.15 1 682 . 62 THR N N 113.4 0.15 1 683 . 62 THR H H 8.83 0.02 1 684 . 62 THR CA C 61.9 0.15 1 685 . 62 THR HA H 4.49 0.02 1 686 . 62 THR CB C 71.0 0.15 1 687 . 62 THR HB H 4.27 0.02 1 688 . 62 THR HG2 H 1.02 0.02 1 689 . 62 THR CG2 C 21.8 0.15 1 690 . 62 THR C C 174.7 0.15 1 691 . 63 ASP N N 123.0 0.15 1 692 . 63 ASP H H 7.27 0.02 1 693 . 63 ASP CA C 53.9 0.15 1 694 . 63 ASP HA H 4.70 0.02 1 695 . 63 ASP CB C 40.4 0.15 1 696 . 63 ASP HB2 H 2.92 0.02 2 697 . 63 ASP HB3 H 2.50 0.02 2 698 . 63 ASP C C 175.2 0.15 1 699 . 64 GLY N N 111.2 0.15 1 700 . 64 GLY H H 8.19 0.02 1 701 . 64 GLY CA C 46.8 0.15 1 702 . 64 GLY HA2 H 3.84 0.02 2 703 . 64 GLY HA3 H 3.53 0.02 2 704 . 64 GLY C C 173.8 0.15 1 705 . 65 ALA N N 118.4 0.15 1 706 . 65 ALA H H 7.99 0.02 1 707 . 65 ALA CA C 52.5 0.15 1 708 . 65 ALA HA H 4.35 0.02 1 709 . 65 ALA HB H 1.41 0.02 1 710 . 65 ALA CB C 19.5 0.15 1 711 . 65 ALA C C 179.1 0.15 1 712 . 66 LYS N N 119.1 0.15 1 713 . 66 LYS H H 7.38 0.02 1 714 . 66 LYS CA C 56.0 0.15 1 715 . 66 LYS HA H 4.34 0.02 1 716 . 66 LYS CB C 35.0 0.15 1 717 . 66 LYS HB2 H 1.91 0.02 2 718 . 66 LYS HB3 H 1.78 0.02 2 719 . 66 LYS CG C 26.4 0.15 1 720 . 66 LYS HG2 H 1.53 0.02 2 721 . 66 LYS HG3 H 1.42 0.02 2 722 . 66 LYS CD C 29.8 0.15 1 723 . 66 LYS HD2 H 1.60 0.02 1 724 . 66 LYS HD3 H 1.60 0.02 1 725 . 66 LYS CE C 42.4 0.15 1 726 . 66 LYS C C 175.1 0.15 1 727 . 67 SER N N 115.0 0.15 1 728 . 67 SER H H 8.69 0.02 1 729 . 67 SER CA C 56.3 0.15 1 730 . 67 SER HA H 4.66 0.02 1 731 . 67 SER CB C 65.8 0.15 1 732 . 67 SER HB2 H 4.36 0.02 2 733 . 67 SER HB3 H 3.88 0.02 2 734 . 67 SER HG H 5.29 0.02 1 735 . 67 SER C C 175.4 0.15 1 736 . 68 LEU N N 117.8 0.15 1 737 . 68 LEU H H 8.49 0.02 1 738 . 68 LEU CA C 58.5 0.15 1 739 . 68 LEU HA H 3.88 0.02 1 740 . 68 LEU CB C 40.0 0.15 1 741 . 68 LEU HB2 H 2.19 0.02 2 742 . 68 LEU HB3 H 1.13 0.02 2 743 . 68 LEU CG C 26.2 0.15 1 744 . 68 LEU HG H 2.19 0.02 1 745 . 68 LEU HD1 H 0.85 0.02 2 746 . 68 LEU HD2 H 0.59 0.02 2 747 . 68 LEU CD1 C 26.0 0.15 1 748 . 68 LEU CD2 C 21.2 0.15 1 749 . 68 LEU C C 179.3 0.15 1 750 . 69 LYS N N 118.4 0.15 1 751 . 69 LYS H H 8.45 0.02 1 752 . 69 LYS CA C 59.5 0.15 1 753 . 69 LYS HA H 4.34 0.02 1 754 . 69 LYS CB C 33.7 0.15 1 755 . 69 LYS HB2 H 1.87 0.02 2 756 . 69 LYS HB3 H 1.55 0.02 2 757 . 69 LYS CG C 24.6 0.15 1 758 . 69 LYS CD C 30.2 0.15 1 759 . 69 LYS HD2 H 1.56 0.02 1 760 . 69 LYS HD3 H 1.56 0.02 1 761 . 69 LYS CE C 42.3 0.15 1 762 . 69 LYS C C 181.3 0.15 1 763 . 70 ASP N N 123.0 0.15 1 764 . 70 ASP H H 8.26 0.02 1 765 . 70 ASP CA C 57.2 0.15 1 766 . 70 ASP HA H 4.39 0.02 1 767 . 70 ASP CB C 40.4 0.15 1 768 . 70 ASP HB2 H 2.92 0.02 2 769 . 70 ASP HB3 H 2.63 0.02 2 770 . 70 ASP C C 178.3 0.15 1 771 . 71 LEU N N 120.4 0.15 1 772 . 71 LEU H H 8.09 0.02 1 773 . 71 LEU CA C 55.5 0.15 1 774 . 71 LEU HA H 4.25 0.02 1 775 . 71 LEU CB C 42.9 0.15 1 776 . 71 LEU HB2 H 1.94 0.02 2 777 . 71 LEU HB3 H 1.75 0.02 2 778 . 71 LEU CG C 28.3 0.15 1 779 . 71 LEU HG H 0.83 0.02 1 780 . 71 LEU HD1 H 1.76 0.02 2 781 . 71 LEU HD2 H 1.06 0.02 2 782 . 71 LEU CD1 C 26.7 0.15 1 783 . 71 LEU CD2 C 23.7 0.15 1 784 . 71 LEU C C 176.3 0.15 1 785 . 72 GLY N N 105.0 0.15 1 786 . 72 GLY H H 7.66 0.02 1 787 . 72 GLY CA C 44.9 0.15 1 788 . 72 GLY HA2 H 4.14 0.02 2 789 . 72 GLY HA3 H 3.48 0.02 2 790 . 72 GLY C C 173.9 0.15 1 791 . 73 VAL N N 120.4 0.15 1 792 . 73 VAL H H 7.70 0.02 1 793 . 73 VAL CA C 64.2 0.15 1 794 . 73 VAL HA H 3.12 0.02 1 795 . 73 VAL CB C 30.8 0.15 1 796 . 73 VAL HB H 1.62 0.02 1 797 . 73 VAL HG1 H 0.91 0.02 2 798 . 73 VAL HG2 H 0.71 0.02 2 799 . 73 VAL CG1 C 22.5 0.15 1 800 . 73 VAL CG2 C 24.4 0.15 1 801 . 73 VAL C C 173.0 0.15 1 802 . 74 ARG N N 121.4 0.15 1 803 . 74 ARG H H 4.92 0.02 1 804 . 74 ARG CA C 51.4 0.15 1 805 . 74 ARG HA H 3.34 0.02 1 806 . 74 ARG CB C 33.8 0.15 1 807 . 74 ARG HB2 H 1.40 0.02 2 808 . 74 ARG HB3 H 0.37 0.02 2 809 . 74 ARG CG C 26.6 0.15 1 810 . 74 ARG HG2 H 1.16 0.02 2 811 . 74 ARG HG3 H 0.95 0.02 2 812 . 74 ARG CD C 43.1 0.15 1 813 . 74 ARG HD2 H 3.32 0.02 2 814 . 74 ARG HD3 H 2.91 0.02 2 815 . 74 ARG C C 173.4 0.15 1 816 . 75 ASP N N 117.0 0.15 1 817 . 75 ASP H H 7.60 0.02 1 818 . 75 ASP CA C 56.7 0.15 1 819 . 75 ASP HA H 4.33 0.02 1 820 . 75 ASP CB C 42.7 0.15 1 821 . 75 ASP HB2 H 2.67 0.02 2 822 . 75 ASP HB3 H 2.60 0.02 2 823 . 75 ASP C C 177.8 0.15 1 824 . 76 GLY N N 110.8 0.15 1 825 . 76 GLY H H 9.25 0.02 1 826 . 76 GLY CA C 45.7 0.15 1 827 . 76 GLY HA2 H 4.20 0.02 2 828 . 76 GLY HA3 H 3.92 0.02 2 829 . 76 GLY C C 174.4 0.15 1 830 . 77 TYR N N 121.4 0.15 1 831 . 77 TYR H H 7.60 0.02 1 832 . 77 TYR CA C 57.0 0.15 1 833 . 77 TYR HA H 4.44 0.02 1 834 . 77 TYR CB C 37.8 0.15 1 835 . 77 TYR HB2 H 3.32 0.02 1 836 . 77 TYR HB3 H 3.32 0.02 1 837 . 77 TYR HD1 H 6.94 0.02 1 838 . 77 TYR HD2 H 6.94 0.02 1 839 . 77 TYR HE1 H 6.84 0.02 1 840 . 77 TYR HE2 H 6.84 0.02 1 841 . 77 TYR CD1 C 131.1 0.15 1 842 . 77 TYR CE1 C 118.8 0.15 1 843 . 77 TYR C C 172.7 0.15 1 844 . 78 ARG N N 119.7 0.15 1 845 . 78 ARG H H 8.81 0.02 1 846 . 78 ARG CA C 53.9 0.15 1 847 . 78 ARG HA H 5.70 0.02 1 848 . 78 ARG CB C 35.1 0.15 1 849 . 78 ARG HB2 H 1.75 0.02 1 850 . 78 ARG HB3 H 1.75 0.02 1 851 . 78 ARG CG C 28.3 0.15 1 852 . 78 ARG HG2 H 1.45 0.02 2 853 . 78 ARG HG3 H 1.13 0.02 2 854 . 78 ARG CD C 43.9 0.15 1 855 . 78 ARG HD2 H 3.10 0.02 2 856 . 78 ARG HD3 H 2.73 0.02 2 857 . 78 ARG C C 175.0 0.15 1 858 . 79 ILE N N 127.3 0.15 1 859 . 79 ILE H H 9.19 0.02 1 860 . 79 ILE CA C 58.7 0.15 1 861 . 79 ILE HA H 4.85 0.02 1 862 . 79 ILE CB C 39.3 0.15 1 863 . 79 ILE HB H 2.02 0.02 1 864 . 79 ILE HG2 H 0.84 0.02 1 865 . 79 ILE CG2 C 17.6 0.15 1 866 . 79 ILE CG1 C 28.0 0.15 1 867 . 79 ILE HG12 H 1.47 0.02 2 868 . 79 ILE HG13 H 1.28 0.02 2 869 . 79 ILE HD1 H 0.71 0.02 1 870 . 79 ILE CD1 C 12.4 0.15 1 871 . 79 ILE C C 173.0 0.15 1 872 . 80 HIS N N 128.1 0.15 1 873 . 80 HIS H H 9.24 0.02 1 874 . 80 HIS CA C 54.2 0.15 1 875 . 80 HIS HA H 5.64 0.02 1 876 . 80 HIS CB C 35.0 0.15 1 877 . 80 HIS HB2 H 3.31 0.02 2 878 . 80 HIS HB3 H 2.60 0.02 2 879 . 80 HIS CD2 C 117.7 0.15 1 880 . 80 HIS CE1 C 137.9 0.15 1 881 . 80 HIS HD2 H 6.99 0.02 1 882 . 80 HIS HE1 H 7.29 0.02 1 883 . 80 HIS C C 174.1 0.15 1 884 . 81 ALA N N 131.7 0.15 1 885 . 81 ALA H H 8.69 0.02 1 886 . 81 ALA CA C 50.1 0.15 1 887 . 81 ALA HA H 5.24 0.02 1 888 . 81 ALA HB H 1.07 0.02 1 889 . 81 ALA CB C 22.1 0.15 1 890 . 81 ALA C C 175.1 0.15 1 891 . 82 VAL N N 118.5 0.15 1 892 . 82 VAL H H 8.62 0.02 1 893 . 82 VAL CA C 60.1 0.15 1 894 . 82 VAL HA H 4.31 0.02 1 895 . 82 VAL CB C 35.7 0.15 1 896 . 82 VAL HB H 1.85 0.02 1 897 . 82 VAL HG1 H 0.70 0.02 2 898 . 82 VAL CG1 C 21.2 0.15 1 899 . 82 VAL C C 175.0 0.15 1 900 . 83 ASP N N 123.7 0.15 1 901 . 83 ASP H H 8.34 0.02 1 902 . 83 ASP CA C 53.0 0.15 1 903 . 83 ASP HA H 4.87 0.02 1 904 . 83 ASP CB C 41.4 0.15 1 905 . 83 ASP HB2 H 2.87 0.02 2 906 . 83 ASP HB3 H 2.45 0.02 2 907 . 83 ASP C C 178.0 0.15 1 908 . 84 VAL N N 122.9 0.15 1 909 . 84 VAL H H 8.66 0.02 1 910 . 84 VAL CA C 62.9 0.15 1 911 . 84 VAL HA H 4.16 0.02 1 912 . 84 VAL CB C 31.7 0.15 1 913 . 84 VAL HB H 2.26 0.02 1 914 . 84 VAL HG1 H 0.85 0.02 2 915 . 84 VAL HG2 H 0.84 0.02 2 916 . 84 VAL CG1 C 22.1 0.15 1 917 . 84 VAL CG2 C 19.2 0.15 1 918 . 84 VAL C C 176.9 0.15 1 919 . 85 THR N N 116.5 0.15 1 920 . 85 THR H H 8.65 0.02 1 921 . 85 THR CA C 63.9 0.15 1 922 . 85 THR HA H 4.19 0.02 1 923 . 85 THR CB C 69.7 0.15 1 924 . 85 THR HB H 4.22 0.02 1 925 . 85 THR HG2 H 1.23 0.02 1 926 . 85 THR CG2 C 22.1 0.15 1 927 . 85 THR C C 176.0 0.15 1 928 . 86 GLY N N 110.9 0.15 1 929 . 86 GLY H H 8.19 0.02 1 930 . 86 GLY CA C 45.6 0.15 1 931 . 86 GLY HA2 H 3.93 0.02 1 932 . 86 GLY HA3 H 3.93 0.02 1 933 . 86 GLY C C 174.6 0.15 1 934 . 87 GLY N N 109.4 0.15 1 935 . 87 GLY H H 8.19 0.02 1 936 . 87 GLY CA C 45.5 0.15 1 937 . 87 GLY HA2 H 3.95 0.02 1 938 . 87 GLY HA3 H 3.95 0.02 1 939 . 87 GLY C C 174.1 0.15 1 940 . 88 ASN N N 118.9 0.15 1 941 . 88 ASN H H 8.35 0.02 1 942 . 88 ASN CA C 53.5 0.15 1 943 . 88 ASN HA H 4.70 0.02 1 944 . 88 ASN CB C 39.3 0.15 1 945 . 88 ASN HB2 H 2.77 0.02 1 946 . 88 ASN HB3 H 2.77 0.02 1 947 . 88 ASN ND2 N 112.8 0.15 1 948 . 88 ASN HD21 H 7.62 0.02 2 949 . 88 ASN HD22 H 6.92 0.02 2 950 . 88 ASN C C 175.6 0.15 1 951 . 89 GLU N N 121.3 0.15 1 952 . 89 GLU H H 8.46 0.02 1 953 . 89 GLU CA C 57.1 0.15 1 954 . 89 GLU HA H 4.17 0.02 1 955 . 89 GLU CB C 30.2 0.15 1 956 . 89 GLU HB2 H 1.88 0.02 1 957 . 89 GLU HB3 H 1.88 0.02 1 958 . 89 GLU CG C 36.5 0.15 1 959 . 89 GLU HG2 H 2.19 0.02 1 960 . 89 GLU HG3 H 2.19 0.02 1 961 . 89 GLU C C 176.2 0.15 1 962 . 90 ASP N N 120.7 0.15 1 963 . 90 ASP H H 8.25 0.02 1 964 . 90 ASP CA C 54.7 0.15 1 965 . 90 ASP HA H 4.49 0.02 1 966 . 90 ASP CB C 41.3 0.15 1 967 . 90 ASP HB2 H 2.55 0.02 2 968 . 90 ASP HB3 H 2.47 0.02 2 969 . 90 ASP C C 175.9 0.15 1 970 . 91 PHE N N 120.7 0.15 1 971 . 91 PHE H H 8.06 0.02 1 972 . 91 PHE CA C 57.9 0.15 1 973 . 91 PHE HA H 4.53 0.02 1 974 . 91 PHE CB C 39.4 0.15 1 975 . 91 PHE HB2 H 3.07 0.02 2 976 . 91 PHE HB3 H 2.97 0.02 2 977 . 91 PHE HD1 H 7.18 0.02 1 978 . 91 PHE HD2 H 7.18 0.02 1 979 . 91 PHE HE1 H 7.28 0.02 1 980 . 91 PHE HE2 H 7.28 0.02 1 981 . 91 PHE CD1 C 131.9 0.15 1 982 . 91 PHE CE1 C 131.8 0.15 1 983 . 91 PHE C C 175.5 0.15 1 984 . 92 LYS N N 123.6 0.15 1 985 . 92 LYS H H 8.04 0.02 1 986 . 92 LYS CA C 56.1 0.15 1 987 . 92 LYS HA H 4.21 0.02 1 988 . 92 LYS CB C 33.5 0.15 1 989 . 92 LYS HB2 H 1.71 0.02 1 990 . 92 LYS HB3 H 1.71 0.02 1 991 . 92 LYS CG C 24.8 0.15 1 992 . 92 LYS HG2 H 1.30 0.02 1 993 . 92 LYS HG3 H 1.30 0.02 1 994 . 92 LYS CD C 29.6 0.15 1 995 . 92 LYS HD2 H 1.64 0.02 1 996 . 92 LYS HD3 H 1.64 0.02 1 997 . 92 LYS CE C 42.5 0.15 1 998 . 92 LYS C C 175.7 0.15 1 999 . 93 ASP N N 122.2 0.15 1 1000 . 93 ASP H H 8.22 0.02 1 1001 . 93 ASP CA C 54.3 0.15 1 1002 . 93 ASP HA H 4.51 0.02 1 1003 . 93 ASP CB C 41.6 0.15 1 1004 . 93 ASP HB2 H 2.70 0.02 2 1005 . 93 ASP HB3 H 2.59 0.02 2 1006 . 93 ASP C C 176.7 0.15 1 1007 . 94 GLU N N 122.9 0.15 1 1008 . 94 GLU H H 8.56 0.02 1 1009 . 94 GLU CA C 57.2 0.15 1 1010 . 94 GLU HA H 4.25 0.02 1 1011 . 94 GLU CB C 30.2 0.15 1 1012 . 94 GLU HB2 H 1.91 0.02 1 1013 . 94 GLU HB3 H 1.91 0.02 1 1014 . 94 GLU CG C 36.5 0.15 1 1015 . 94 GLU HG2 H 2.23 0.02 1 1016 . 94 GLU HG3 H 2.23 0.02 1 1017 . 94 GLU C C 176.9 0.15 1 1018 . 95 SER N N 116.5 0.15 1 1019 . 95 SER H H 8.42 0.02 1 1020 . 95 SER CA C 59.5 0.15 1 1021 . 95 SER HA H 4.32 0.02 1 1022 . 95 SER CB C 64.1 0.15 1 1023 . 95 SER HB2 H 3.87 0.02 1 1024 . 95 SER HB3 H 3.87 0.02 1 1025 . 95 SER C C 174.9 0.15 1 1026 . 96 MET N N 122.2 0.15 1 1027 . 96 MET H H 8.18 0.02 1 1028 . 96 MET CA C 55.8 0.15 1 1029 . 96 MET HA H 4.50 0.02 1 1030 . 96 MET CB C 33.0 0.15 1 1031 . 96 MET HB2 H 2.52 0.02 1 1032 . 96 MET HB3 H 2.52 0.02 1 1033 . 96 MET CG C 32.5 0.15 1 1034 . 96 MET HG2 H 2.04 0.02 1 1035 . 96 MET HG3 H 2.04 0.02 1 1036 . 96 MET C C 176.2 0.15 1 1037 . 97 VAL N N 120.9 0.15 1 1038 . 97 VAL H H 7.85 0.02 1 1039 . 97 VAL CA C 62.6 0.15 1 1040 . 97 VAL HA H 4.00 0.02 1 1041 . 97 VAL CB C 33.2 0.15 1 1042 . 97 VAL HB H 2.03 0.02 1 1043 . 97 VAL HG1 H 0.91 0.02 2 1044 . 97 VAL CG1 C 21.2 0.15 1 1045 . 97 VAL C C 176.2 0.15 1 1046 . 98 GLU N N 124.5 0.15 1 1047 . 98 GLU H H 8.40 0.02 1 1048 . 98 GLU CA C 56.9 0.15 1 1049 . 98 GLU HA H 4.17 0.02 1 1050 . 98 GLU CB C 30.4 0.15 1 1051 . 98 GLU HB2 H 1.88 0.02 1 1052 . 98 GLU HB3 H 1.88 0.02 1 1053 . 98 GLU CG C 36.5 0.15 1 1054 . 98 GLU HG2 H 2.18 0.02 1 1055 . 98 GLU HG3 H 2.18 0.02 1 1056 . 98 GLU C C 176.2 0.15 1 1057 . 99 LYS N N 122.5 0.15 1 1058 . 99 LYS H H 8.18 0.02 1 1059 . 99 LYS CA C 56.3 0.15 1 1060 . 99 LYS HA H 4.21 0.02 1 1061 . 99 LYS CB C 33.4 0.15 1 1062 . 99 LYS HB2 H 2.02 0.02 1 1063 . 99 LYS HB3 H 2.02 0.02 1 1064 . 99 LYS CG C 24.9 0.15 1 1065 . 99 LYS HG2 H 1.28 0.02 1 1066 . 99 LYS HG3 H 1.28 0.02 1 1067 . 99 LYS CD C 29.5 0.15 1 1068 . 99 LYS HD2 H 1.66 0.02 1 1069 . 99 LYS HD3 H 1.66 0.02 1 1070 . 99 LYS CE C 42.3 0.15 1 1071 . 99 LYS HE2 H 2.61 0.02 1 1072 . 99 LYS HE3 H 2.61 0.02 1 1073 . 99 LYS C C 176.2 0.15 1 1074 . 100 TYR N N 121.3 0.15 1 1075 . 100 TYR H H 8.14 0.02 1 1076 . 100 TYR CA C 57.7 0.15 1 1077 . 100 TYR HA H 4.54 0.02 1 1078 . 100 TYR CB C 39.0 0.15 1 1079 . 100 TYR HB2 H 3.00 0.02 2 1080 . 100 TYR HB3 H 2.88 0.02 2 1081 . 100 TYR HD1 H 7.06 0.02 1 1082 . 100 TYR HD2 H 7.06 0.02 1 1083 . 100 TYR HE1 H 6.76 0.02 1 1084 . 100 TYR HE2 H 6.76 0.02 1 1085 . 100 TYR CD1 C 133.3 0.15 1 1086 . 100 TYR CE1 C 118.3 0.15 1 1087 . 100 TYR C C 175.7 0.15 1 1088 . 101 GLU N N 123.0 0.15 1 1089 . 101 GLU H H 8.34 0.02 1 1090 . 101 GLU CA C 56.4 0.15 1 1091 . 101 GLU HA H 4.24 0.02 1 1092 . 101 GLU CB C 30.7 0.15 1 1093 . 101 GLU HB2 H 1.89 0.02 1 1094 . 101 GLU HB3 H 1.89 0.02 1 1095 . 101 GLU CG C 36.4 0.15 1 1096 . 101 GLU HG2 H 2.18 0.02 1 1097 . 101 GLU HG3 H 2.18 0.02 1 1098 . 101 GLU C C 176.2 0.15 1 1099 . 102 MET N N 121.7 0.15 1 1100 . 102 MET H H 8.30 0.02 1 1101 . 102 MET CA C 55.6 0.15 1 1102 . 102 MET HA H 4.45 0.02 1 1103 . 102 MET CB C 33.0 0.15 1 1104 . 102 MET HB2 H 2.63 0.02 1 1105 . 102 MET HB3 H 2.63 0.02 1 1106 . 102 MET CG C 32.7 0.15 1 1107 . 102 MET HG2 H 2.00 0.02 1 1108 . 102 MET HG3 H 2.00 0.02 1 1109 . 102 MET C C 176.2 0.15 1 1110 . 103 SER N N 117.1 0.15 1 1111 . 103 SER H H 8.28 0.02 1 1112 . 103 SER CA C 58.5 0.15 1 1113 . 103 SER HA H 4.42 0.02 1 1114 . 103 SER CB C 64.4 0.15 1 1115 . 103 SER HB2 H 3.84 0.02 1 1116 . 103 SER HB3 H 3.84 0.02 1 1117 . 103 SER C C 174.3 0.15 1 1118 . 104 ASP N N 122.7 0.15 1 1119 . 104 ASP H H 8.37 0.02 1 1120 . 104 ASP CA C 54.7 0.15 1 1121 . 104 ASP CB C 41.6 0.15 1 1122 . 104 ASP C C 176.3 0.15 1 1123 . 105 ASP N N 121.2 0.15 1 1124 . 105 ASP H H 8.35 0.02 1 1125 . 105 ASP CA C 54.8 0.15 1 1126 . 105 ASP HA H 4.59 0.02 1 1127 . 105 ASP CB C 41.3 0.15 1 1128 . 105 ASP HB2 H 2.65 0.02 1 1129 . 105 ASP HB3 H 2.65 0.02 1 1130 . 105 ASP C C 176.9 0.15 1 1131 . 106 THR N N 114.1 0.15 1 1132 . 106 THR H H 8.10 0.02 1 1133 . 106 THR CA C 63.3 0.15 1 1134 . 106 THR HA H 4.09 0.02 1 1135 . 106 THR CB C 69.7 0.15 1 1136 . 106 THR HB H 4.06 0.02 1 1137 . 106 THR HG2 H 1.01 0.02 1 1138 . 106 THR CG2 C 21.8 0.15 1 1139 . 106 THR C C 175.0 0.15 1 1140 . 107 TYR N N 121.7 0.15 1 1141 . 107 TYR H H 8.16 0.02 1 1142 . 107 TYR CA C 59.0 0.15 1 1143 . 107 TYR HA H 4.42 0.02 1 1144 . 107 TYR CB C 38.6 0.15 1 1145 . 107 TYR HB2 H 3.06 0.02 2 1146 . 107 TYR HB3 H 2.95 0.02 2 1147 . 107 TYR HD1 H 7.08 0.02 1 1148 . 107 TYR HD2 H 7.08 0.02 1 1149 . 107 TYR HE1 H 6.78 0.02 1 1150 . 107 TYR HE2 H 6.78 0.02 1 1151 . 107 TYR CD1 C 133.3 0.15 1 1152 . 107 TYR CE1 C 118.3 0.15 1 1153 . 107 TYR C C 176.7 0.15 1 1154 . 108 GLY N N 110.4 0.15 1 1155 . 108 GLY H H 8.18 0.02 1 1156 . 108 GLY CA C 45.6 0.15 1 1157 . 108 GLY HA2 H 3.87 0.02 2 1158 . 108 GLY HA3 H 3.80 0.02 2 1159 . 108 GLY C C 174.1 0.15 1 1160 . 109 LYS N N 120.6 0.15 1 1161 . 109 LYS H H 8.01 0.02 1 1162 . 109 LYS CA C 56.4 0.15 1 1163 . 109 LYS HA H 4.29 0.02 1 1164 . 109 LYS CB C 33.2 0.15 1 1165 . 109 LYS HB2 H 1.75 0.02 1 1166 . 109 LYS HB3 H 1.75 0.02 1 1167 . 109 LYS CG C 25.0 0.15 1 1168 . 109 LYS HG2 H 1.35 0.02 1 1169 . 109 LYS HG3 H 1.35 0.02 1 1170 . 109 LYS CD C 29.5 0.15 1 1171 . 109 LYS HD2 H 1.71 0.02 1 1172 . 109 LYS HD3 H 1.71 0.02 1 1173 . 109 LYS CE C 42.3 0.15 1 1174 . 109 LYS C C 176.9 0.15 1 1175 . 110 ARG N N 122.5 0.15 1 1176 . 110 ARG H H 8.40 0.02 1 1177 . 110 ARG CA C 56.5 0.15 1 1178 . 110 ARG HA H 4.38 0.02 1 1179 . 110 ARG CB C 31.1 0.15 1 1180 . 110 ARG CG C 26.7 0.15 1 1181 . 110 ARG CD C 43.6 0.15 1 1182 . 110 ARG C C 176.9 0.15 1 1183 . 111 THR N N 114.9 0.15 1 1184 . 111 THR H H 8.23 0.02 1 1185 . 111 THR CA C 62.1 0.15 1 1186 . 111 THR HA H 4.28 0.02 1 1187 . 111 THR CB C 70.1 0.15 1 1188 . 111 THR HG2 H 1.16 0.02 1 1189 . 111 THR CG2 C 21.7 0.15 1 1190 . 111 THR C C 174.5 0.15 1 1191 . 112 ASP N N 122.5 0.15 1 1192 . 112 ASP H H 8.34 0.02 1 1193 . 112 ASP CA C 54.5 0.15 1 1194 . 112 ASP HA H 4.59 0.02 1 1195 . 112 ASP CB C 41.5 0.15 1 1196 . 112 ASP HB2 H 2.65 0.02 1 1197 . 112 ASP HB3 H 2.65 0.02 1 1198 . 112 ASP C C 176.3 0.15 1 1199 . 113 SER N N 115.8 0.15 1 1200 . 113 SER H H 8.16 0.02 1 1201 . 113 SER CA C 58.8 0.15 1 1202 . 113 SER HA H 4.42 0.02 1 1203 . 113 SER CB C 63.9 0.15 1 1204 . 113 SER HB2 H 3.83 0.02 1 1205 . 113 SER HB3 H 3.83 0.02 1 1206 . 113 SER C C 174.7 0.15 1 1207 . 114 VAL N N 121.8 0.15 1 1208 . 114 VAL H H 8.05 0.02 1 1209 . 114 VAL CA C 62.9 0.15 1 1210 . 114 VAL HA H 4.02 0.02 1 1211 . 114 VAL CB C 33.1 0.15 1 1212 . 114 VAL HB H 2.03 0.02 1 1213 . 114 VAL HG1 H 0.88 0.02 2 1214 . 114 VAL CG1 C 21.3 0.15 1 1215 . 114 VAL C C 176.4 0.15 1 1216 . 115 ARG N N 124.0 0.15 1 1217 . 115 ARG H H 8.21 0.02 1 1218 . 115 ARG CA C 56.2 0.15 1 1219 . 115 ARG HA H 4.14 0.02 1 1220 . 115 ARG CB C 31.0 0.15 1 1221 . 115 ARG HB2 H 1.58 0.02 1 1222 . 115 ARG HB3 H 1.58 0.02 1 1223 . 115 ARG C C 176.0 0.15 1 1224 . 116 ALA N N 124.7 0.15 1 1225 . 116 ALA H H 8.15 0.02 1 1226 . 116 ALA CA C 52.7 0.15 1 1227 . 116 ALA HA H 4.22 0.02 1 1228 . 116 ALA HB H 1.27 0.02 1 1229 . 116 ALA CB C 19.2 0.15 1 1230 . 116 ALA C C 177.3 0.15 1 1231 . 117 TRP N N 120.1 0.15 1 1232 . 117 TRP H H 7.95 0.02 1 1233 . 117 TRP CA C 57.3 0.15 1 1234 . 117 TRP HA H 4.61 0.02 1 1235 . 117 TRP CB C 29.8 0.15 1 1236 . 117 TRP HB2 H 3.22 0.02 1 1237 . 117 TRP HB3 H 3.22 0.02 1 1238 . 117 TRP CD1 C 127.3 0.15 1 1239 . 117 TRP NE1 N 129.6 0.15 1 1240 . 117 TRP HD1 H 7.19 0.02 1 1241 . 117 TRP CZ2 C 114.6 0.15 1 1242 . 117 TRP HE1 H 10.10 0.02 1 1243 . 117 TRP CH2 C 124.6 0.15 1 1244 . 117 TRP HZ2 H 7.43 0.02 1 1245 . 117 TRP HH2 H 7.17 0.02 1 1246 . 117 TRP C C 175.9 0.15 1 1247 . 118 LYS N N 123.1 0.15 1 1248 . 118 LYS H H 7.87 0.02 1 1249 . 118 LYS CA C 56.0 0.15 1 1250 . 118 LYS HA H 4.17 0.02 1 1251 . 118 LYS CB C 33.7 0.15 1 1252 . 118 LYS HB2 H 1.66 0.02 1 1253 . 118 LYS HB3 H 1.66 0.02 1 1254 . 118 LYS CG C 24.7 0.15 1 1255 . 118 LYS HG2 H 1.18 0.02 1 1256 . 118 LYS HG3 H 1.18 0.02 1 1257 . 118 LYS CD C 29.6 0.15 1 1258 . 118 LYS HD2 H 1.53 0.02 1 1259 . 118 LYS HD3 H 1.53 0.02 1 1260 . 118 LYS CE C 42.3 0.15 1 1261 . 118 LYS C C 175.7 0.15 1 1262 . 119 LYS N N 123.7 0.15 1 1263 . 119 LYS H H 8.11 0.02 1 1264 . 119 LYS CA C 56.7 0.15 1 1265 . 119 LYS HA H 4.12 0.02 1 1266 . 119 LYS CB C 33.3 0.15 1 1267 . 119 LYS HB2 H 1.72 0.02 1 1268 . 119 LYS HB3 H 1.72 0.02 1 1269 . 119 LYS CG C 24.8 0.15 1 1270 . 119 LYS HG2 H 1.39 0.02 1 1271 . 119 LYS HG3 H 1.39 0.02 1 1272 . 119 LYS CD C 29.4 0.15 1 1273 . 119 LYS HD2 H 1.64 0.02 1 1274 . 119 LYS HD3 H 1.64 0.02 1 1275 . 119 LYS CE C 42.3 0.15 1 1276 . 119 LYS C C 175.6 0.15 1 1277 . 120 LYS N N 128.4 0.15 1 1278 . 120 LYS H H 7.92 0.02 1 1279 . 120 LYS CA C 58.0 0.15 1 1280 . 120 LYS HA H 4.09 0.02 1 1281 . 120 LYS CB C 34.2 0.15 1 1282 . 120 LYS HB2 H 1.72 0.02 1 1283 . 120 LYS HB3 H 1.72 0.02 1 1284 . 120 LYS HG2 H 1.33 0.02 1 1285 . 120 LYS HG3 H 1.33 0.02 1 1286 . 120 LYS HD2 H 1.64 0.02 1 1287 . 120 LYS HD3 H 1.64 0.02 1 1288 . 120 LYS C C 181.3 0.15 1 stop_ save_